메뉴 건너뛰기




Volumn 17, Issue 7, 2000, Pages 989-1000

Enolase from Trypanosoma brucei, from the amitochondriate protist Mastigamoeba balamuthi, and from the chloroplast and cytosol of Euglena gracilis: Pieces in the evolutionary puzzle of the eukaryotic glycolytic pathway

Author keywords

Amitochondriate protist; Endosymbiosis; Evolution; Glycolysis; Metabolism; Organelles; Phylogeny

Indexed keywords

ENOLASE;

EID: 0033947724     PISSN: 07374038     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.molbev.a026395     Document Type: Article
Times cited : (63)

References (81)
  • 1
    • 0002367729 scopus 로고    scopus 로고
    • MOLPHY version 2.3: Programs for molecular phylogenetics based on maximum likelihood
    • ADACHI, J., and M. HASEGAWA. 1996. MOLPHY version 2.3: programs for molecular phylogenetics based on maximum likelihood. Comput. Sci. Monogr. 28:1-150.
    • (1996) Comput. Sci. Monogr. , vol.28 , pp. 1-150
    • Adachi, J.1    Hasegawa, M.2
  • 2
    • 0032517093 scopus 로고    scopus 로고
    • Molecular analysis of phosphoglycerate kinase in Trypanoplasma borreli and the evolution of this enzyme in Kinetoplastida
    • ADJÉ, C., F. R. OPPERDOES, and P. A. M. MICHELS. 1998. Molecular analysis of phosphoglycerate kinase in Trypanoplasma borreli and the evolution of this enzyme in Kinetoplastida. Gene 217:91-99.
    • (1998) Gene , vol.217 , pp. 91-99
    • Adjé, C.1    Opperdoes, F.R.2    Michels, P.A.M.3
  • 3
    • 0031021873 scopus 로고    scopus 로고
    • Glycolysis in bloodstream form Trypanosoma brucei can be understood in terms of the kinetics of the glycolytic enzymes
    • BAKKER, B. M., P. A. M. MICHELS, F. R. OPPERDOES, and H. V. WESTERHOFF. 1997. Glycolysis in bloodstream form Trypanosoma brucei can be understood in terms of the kinetics of the glycolytic enzymes. J. Biol. Chem. 272:3207-3215.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3207-3215
    • Bakker, B.M.1    Michels, P.A.M.2    Opperdoes, F.R.3    Westerhoff, H.V.4
  • 4
    • 0030037573 scopus 로고    scopus 로고
    • Higher plant chloroplast and cytosolic 3-phosphoglycerate kinases: A case of endosymbiotic gene replacement
    • BRINKMANN, H., and W. MARTIN. 1996. Higher plant chloroplast and cytosolic 3-phosphoglycerate kinases: a case of endosymbiotic gene replacement. Plant Mol. Biol. 30:65-75.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 65-75
    • Brinkmann, H.1    Martin, W.2
  • 5
    • 0032422012 scopus 로고    scopus 로고
    • A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis
    • BROWN, C. K., P. L. KUHLMAN, S. MATTINGLY, K. SLATES, P. J. CALIE, and W. W. FARRAR. 1998. A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis. Protein Chem. 17:855-866.
    • (1998) Protein Chem. , vol.17 , pp. 855-866
    • Brown, C.K.1    Kuhlman, P.L.2    Mattingly, S.3    Slates, K.4    Calie, P.J.5    Farrar, W.W.6
  • 6
    • 0031470387 scopus 로고    scopus 로고
    • Archaea and the prokaryote-to-eukaryote transition
    • BROWN, J. R., and W. F. DOOLITTLE. 1997. Archaea and the prokaryote-to-eukaryote transition. Microbiol. Mol. Biol. Rev. 61:456-502.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 456-502
    • Brown, J.R.1    Doolittle, W.F.2
  • 7
    • 84987471865 scopus 로고
    • Evolution and diversity of amitochondrial zooflagellates
    • BRUGEROLLE, G. 1993. Evolution and diversity of amitochondrial zooflagellates. J. Eukaryot. Microbiol. 40:616-618.
    • (1993) J. Eukaryot. Microbiol. , vol.40 , pp. 616-618
    • Brugerolle, G.1
  • 8
    • 0025875099 scopus 로고
    • Archamoebae: The ancestral eukaryotes?
    • CAVALIER-SMITH, T. 1991. Archamoebae: the ancestral eukaryotes? BioSystems 25:25-38.
    • (1991) Biosystems , vol.25 , pp. 25-38
    • Cavalier-Smith, T.1
  • 9
    • 0027145102 scopus 로고
    • Kingdom protozoa and its 18 phyla
    • _. 1993. Kingdom protozoa and its 18 phyla. Microbiol. Rev. 57:953-994.
    • (1993) Microbiol. Rev. , vol.57 , pp. 953-994
  • 10
    • 0022761834 scopus 로고
    • A light and electron microscopical study of a new, polymorphic free-living amoeba, Phreatamoeba balamuthi n.g., n.sp
    • CHAVÉZ, L. A., W. BALAMUTH, and T. GONG. 1986. A light and electron microscopical study of a new, polymorphic free-living amoeba, Phreatamoeba balamuthi n.g., n.sp. J. Protozool. 33:397-404.
    • (1986) J. Protozool. , vol.33 , pp. 397-404
    • Chavéz, L.A.1    Balamuth, W.2    Gong, T.3
  • 11
    • 0030560864 scopus 로고    scopus 로고
    • Metabolic compartmentation in African trypanosomes
    • CLAYTON, C. E., and P. MICHELS. 1996. Metabolic compartmentation in African trypanosomes. Parasitol. Today 12: 465-471.
    • (1996) Parasitol. Today , vol.12 , pp. 465-471
    • Clayton, C.E.1    Michels, P.2
  • 12
    • 0028047203 scopus 로고
    • Molecular cloning and nucleotide sequences of cDNAs encoding subunits I, II, and IX of Euglena gracilis mitochondrial complex III
    • Cui, J.-Y., K. MUKAI, K. SAEKI, and H. MATSUBARA. 1994. Molecular cloning and nucleotide sequences of cDNAs encoding subunits I, II, and IX of Euglena gracilis mitochondrial complex III. J. Biochem. (Tokyo) 115:98-107.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 98-107
    • Cui, J.-Y.1    Mukai, K.2    Saeki, K.3    Matsubara, H.4
  • 13
    • 0032485497 scopus 로고    scopus 로고
    • A paradigm gets shifty
    • DOOLITTLE, W. F. 1998. A paradigm gets shifty. Nature 392: 15-16.
    • (1998) Nature , vol.392 , pp. 15-16
    • Doolittle, W.F.1
  • 14
    • 0033603539 scopus 로고    scopus 로고
    • Phylogenetic classification and the universal tree
    • _. 1999. Phylogenetic classification and the universal tree. Science 284:2124-2128.
    • (1999) Science , vol.284 , pp. 2124-2128
  • 15
    • 0028871609 scopus 로고
    • X-ray structure and catalytic mechanism of lobster enolase
    • DUQUERROY, S., C. CAMUS, and J. JANIN. 1995. X-ray structure and catalytic mechanism of lobster enolase. Biochemistry 34:12513-12523.
    • (1995) Biochemistry , vol.34 , pp. 12513-12523
    • Duquerroy, S.1    Camus, C.2    Janin, J.3
  • 16
    • 0033609934 scopus 로고    scopus 로고
    • The protozoan parasite Toxoplasma gondii expresses two functional plant-like glycolytic enzymes
    • DZIERSZINSKI, F., O. POPESCU, C. TOURSEL, C. SLOMIANNY, B. YAHIAOUI, and S. TOMAVO. 1999. The protozoan parasite Toxoplasma gondii expresses two functional plant-like glycolytic enzymes. J. Biol. Chem. 274:24888-24895.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24888-24895
    • Dzierszinski, F.1    Popescu, O.2    Toursel, C.3    Slomianny, C.4    Yahiaoui, B.5    Tomavo, S.6
  • 18
    • 0032949947 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: Evidence of intra- and inter-kingdom gene transfer
    • FIGGE, R. M., M. SCHUBERT, H. BRINKMANN, and R. CERFF. 1999. Glyceraldehyde-3-phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: evidence of intra- and inter-kingdom gene transfer. Mol. Biol. Evol. 16:429-440.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 429-440
    • Figge, R.M.1    Schubert, M.2    Brinkmann, H.3    Cerff, R.4
  • 20
    • 0001030798 scopus 로고
    • The chloroplasts of Euglena may have evolved from symbiotic green algae
    • GIBBS, S. P. 1978. The chloroplasts of Euglena may have evolved from symbiotic green algae. Can. J. Bot. 56:2883-2889.
    • (1978) Can. J. Bot. , vol.56 , pp. 2883-2889
    • Gibbs, S.P.1
  • 21
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • GRAY, M. W., G. BURGER, and B. F. LANG. 1999. Mitochondrial evolution. Science 283:1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 22
    • 0028180653 scopus 로고
    • Structure, function and biogenesis of glycosomes in Kinetoplastida
    • HANNAERT, V., and P. MICHELS. 1994. Structure, function and biogenesis of glycosomes in Kinetoplastida. J. Bioenerg. Biomembr. 20:205-212.
    • (1994) J. Bioenerg. Biomembr. , vol.20 , pp. 205-212
    • Hannaert, V.1    Michels, P.2
  • 23
    • 0029047354 scopus 로고
    • A nuclear gene of eubacterial origin in Euglena gracilis reflects cryptic endosymbioses during protist evolution
    • HENZE, K., A. BADR, M. WETTERN, R. CERFF, and W. MARTIN. 1995. A nuclear gene of eubacterial origin in Euglena gracilis reflects cryptic endosymbioses during protist evolution. Proc. Natl. Acad. Sci. USA 92:9122-9126.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9122-9126
    • Henze, K.1    Badr, A.2    Wettern, M.3    Cerff, R.4    Martin, W.5
  • 24
    • 0032548159 scopus 로고    scopus 로고
    • Sequence and phylogenetic position of a class II aldolase gene in the amitochondriate protist, Giardia lamblia
    • HENZE, K., H. G. MORRISON, M. L. SOGIN, and M. MÜLLER. 1998. Sequence and phylogenetic position of a class II aldolase gene in the amitochondriate protist, Giardia lamblia. Gene 222:163-168.
    • (1998) Gene , vol.222 , pp. 163-168
    • Henze, K.1    Morrison, H.G.2    Sogin, M.L.3    Müller, M.4
  • 25
    • 0028359393 scopus 로고
    • The unusually long small subunit ribosomal RNA of Phreatamoeba balamuthi
    • HINKLE, G., D. D. LEIPE, T. A. NERAD, and M. L. SOGIN. 1994. The unusually long small subunit ribosomal RNA of Phreatamoeba balamuthi. Nucleic Acids Res. 22:465-469.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 465-469
    • Hinkle, G.1    Leipe, D.D.2    Nerad, T.A.3    Sogin, M.L.4
  • 26
    • 0000422713 scopus 로고
    • The plastidic 3-phosphoglycerate → acetylCoA pathway in barley leaves and its involvement in the synthesis of amino acids, plastidic isoprenoids and fatty acids during chloroplast development
    • HOPPE, P., A. HEINTZE, A. RIEDEL, C. CREUZER, and G. SCHULTZ. 1993. The plastidic 3-phosphoglycerate → acetylCoA pathway in barley leaves and its involvement in the synthesis of amino acids, plastidic isoprenoids and fatty acids during chloroplast development. Planta 190:253-262.
    • (1993) Planta , vol.190 , pp. 253-262
    • Hoppe, P.1    Heintze, A.2    Riedel, A.3    Creuzer, C.4    Schultz, G.5
  • 27
    • 0021984720 scopus 로고
    • Yeast heat shock protein of Mr 48,000 is an isoprotein of enolase
    • IIDA, H., and I. YAHARA. 1985. Yeast heat shock protein of Mr 48,000 is an isoprotein of enolase. Nature 315:688-690.
    • (1985) Nature , vol.315 , pp. 688-690
    • Iida, H.1    Yahara, I.2
  • 28
    • 0031038402 scopus 로고    scopus 로고
    • Evidence that eukaryotic triosphosphate isomerase is of alpha-proteobacterial origin
    • KEELING, P. J., and W. F. DOOLITTLE. 1997. Evidence that eukaryotic triosphosphate isomerase is of alpha-proteobacterial origin. Proc. Natl. Acad. Sci. USA 94:1270-1275.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1270-1275
    • Keeling, P.J.1    Doolittle, W.F.2
  • 30
    • 0029925438 scopus 로고    scopus 로고
    • Cloning and characterization of the NAD-linked glycerol-3-phosphate dehydrogenases of Trypanosoma brucei and Leishmania mexicana mexicana and expression of the trypanosome enzyme in Escherichia coli
    • KOHL, L., T. DRMOTA, C.-D. Do-THI, M. CALLENS, J. VAN BEEUMEN, F. R. OPPERDOES, and P. A. M. MICHELS. 1996. Cloning and characterization of the NAD-linked glycerol-3-phosphate dehydrogenases of Trypanosoma brucei and Leishmania mexicana mexicana and expression of the trypanosome enzyme in Escherichia coli. Mol. Biochem. Parasitol. 76:159-173.
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 159-173
    • Kohl, L.1    Drmota, T.2    Do-Thi, C.-D.3    Callens, M.4    Van Beeumen, J.5    Opperdoes, F.R.6    Michels, P.A.M.7
  • 32
    • 0001717905 scopus 로고
    • Enzyme activities of the carbon reduction cycle in some photosynthetic organisms
    • LATZKO, E., and M. GIBBS. 1969. Enzyme activities of the carbon reduction cycle in some photosynthetic organisms. Plant Physiol. 44:295-300.
    • (1969) Plant Physiol. , vol.44 , pp. 295-300
    • Latzko, E.1    Gibbs, M.2
  • 33
    • 0032482924 scopus 로고    scopus 로고
    • Molecular archaeology of the Escherichia coli genome
    • LAWRENCE, J. G., and H. OCHMAN. 1998. Molecular archaeology of the Escherichia coli genome. Proc. Natl. Acad. Sci. USA 95:9413-9417.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9413-9417
    • Lawrence, J.G.1    Ochman, H.2
  • 34
    • 0028504314 scopus 로고
    • Tubulin genes in the algal protist Euglena gracilis
    • LEVASSEUR, P. J., Q. MENG, and B. BOUCK. 1994. Tubulin genes in the algal protist Euglena gracilis. J. Eukaryot. Microbiol. 41:468-477.
    • (1994) J. Eukaryot. Microbiol. , vol.41 , pp. 468-477
    • Levasseur, P.J.1    Meng, Q.2    Bouck, B.3
  • 36
    • 0020490759 scopus 로고
    • Targeted deletion of a yeast enolase structural gene
    • MCALISTER, L., and M. J. HOLLAND. 1982. Targeted deletion of a yeast enolase structural gene. J. Biol. Chem. 257:7181-7188.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7181-7188
    • McAlister, L.1    Holland, M.J.2
  • 38
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • MCFADDEN, G. I., and D. ROOS. 1999. Apicomplexan plastids as drug targets. Trends Microbiol. 7:328-332.
    • (1999) Trends Microbiol. , vol.7 , pp. 328-332
    • McFadden, G.I.1    Roos, D.2
  • 39
    • 0027423316 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochoridriate eukaryote Trichomonas vaginalis
    • MARKOS, A., A. MIRETSKY, and M. MÜLLER. 1993. A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochoridriate eukaryote Trichomonas vaginalis. J. Mol. Evol. 37:631-643.
    • (1993) J. Mol. Evol. , vol.37 , pp. 631-643
    • Markos, A.1    Miretsky, A.2    Müller, M.3
  • 40
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis of the first eukaryote
    • MARTIN, W., and M. MÜLLER. 1998. The hydrogen hypothesis of the first eukaryote. Nature 392:37-41.
    • (1998) Nature , vol.392 , pp. 37-41
    • Martin, W.1    Müller, M.2
  • 41
    • 0030850422 scopus 로고    scopus 로고
    • The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: A case study of functional redundancy in ancient pathways through endosymbiosis
    • MARTIN, W., and C. SCHNARRENBERGER. 1997. The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: a case study of functional redundancy in ancient pathways through endosymbiosis. Curr. Genet. 32:1-18.
    • (1997) Curr. Genet. , vol.32 , pp. 1-18
    • Martin, W.1    Schnarrenberger, C.2
  • 43
    • 0027412292 scopus 로고
    • ATP versus pyrophosphate: Glycolysis revisited in parasitic protists
    • MERTENS, E. 1993. ATP versus pyrophosphate: glycolysis revisited in parasitic protists. Parasitol. Today 9:122-126.
    • (1993) Parasitol. Today , vol.9 , pp. 122-126
    • Mertens, E.1
  • 44
    • 0032429638 scopus 로고    scopus 로고
    • The pyrophosphate-dependent phosphofructokinase of the protist, Trichomonas vaginalis, and the evolutionary relationships of protist phosphofructokinases
    • MERTENS, E., U. S. LADROR, J. A. LEE, A. MIRETSKY, A. MORRIS, C. ROZARIO, R. J. KEMP, and M. MÜLLER. 1998. The pyrophosphate-dependent phosphofructokinase of the protist, Trichomonas vaginalis, and the evolutionary relationships of protist phosphofructokinases. J. Mol. Evol. 47: 739-750.
    • (1998) J. Mol. Evol. , vol.47 , pp. 739-750
    • Mertens, E.1    Ladror, U.S.2    Lee, J.A.3    Miretsky, A.4    Morris, A.5    Rozario, C.6    Kemp, R.J.7    Müller, M.8
  • 45
    • 0026717685 scopus 로고
    • Pyruvate kinase from Trichomonas vaginalis, an allosteric enzyme stimulated by ribose 5-phosphate and glycerate 3-phosphate
    • MERTENS, E., E. VAN SCHAFTINGEN, and M. MÜLLER. 1992. Pyruvate kinase from Trichomonas vaginalis, an allosteric enzyme stimulated by ribose 5-phosphate and glycerate 3-phosphate. Mol. Biochem. Parasitol. 54:13-20.
    • (1992) Mol. Biochem. Parasitol. , vol.54 , pp. 13-20
    • Mertens, E.1    Van Schaftingen, E.2    Müller, M.3
  • 46
    • 0031574041 scopus 로고    scopus 로고
    • The glycosomal ATP-dependent phosphofructokinase of Trypanosoma brucei must have evolved from an ancestral pyrophosphate-dependent enzyme
    • MICHELS, P. A. M., N. CHEVALIER, F. R. OPPERDOES, M. H. RIDER, and D. J. RIGDEN. 1997. The glycosomal ATP-dependent phosphofructokinase of Trypanosoma brucei must have evolved from an ancestral pyrophosphate-dependent enzyme. Eur. J. Biochem. 250:698-704.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 698-704
    • Michels, P.A.M.1    Chevalier, N.2    Opperdoes, F.R.3    Rider, M.H.4    Rigden, D.J.5
  • 47
    • 0028348247 scopus 로고
    • The evolution of kinetoplastid glycosomes
    • MICHELS, P. A. M., and V. HANNAERT. 1994. The evolution of kinetoplastid glycosomes. J. Bioenerg. Biomembr. 26:213-219.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 213-219
    • Michels, P.A.M.1    Hannaert, V.2
  • 48
    • 0013636622 scopus 로고
    • The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma brucei have a distinct evolutionary relationship
    • MICHELS, P. A. M., M. MARCHAND, L. KOHL, S. ALLERT, R. K. WIERENGA, and F. R. OPPERDOES. 1991. The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma brucei have a distinct evolutionary relationship. Eur. J. Biochem. 200:19-27.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 19-27
    • Michels, P.A.M.1    Marchand, M.2    Kohl, L.3    Allert, S.4    Wierenga, R.K.5    Opperdoes, F.R.6
  • 49
    • 0040491944 scopus 로고
    • A developmental analysis of the enolase isozymes from Ricinus communis
    • MIERNYK, J. A., and D. T. DENNIS. 1992. A developmental analysis of the enolase isozymes from Ricinus communis. Plant Physiol. 99:748-750.
    • (1992) Plant Physiol. , vol.99 , pp. 748-750
    • Miernyk, J.A.1    Dennis, D.T.2
  • 50
    • 0015653828 scopus 로고
    • Triosephosphate isomerase and aldolases from light and dark-grown Euglena gracilis
    • Mo, Y., B. G. HARRIS, and R. W. GRACY. 1973. Triosephosphate isomerase and aldolases from light and dark-grown Euglena gracilis. Arch. Biochem. Biophys. 157:580-587.
    • (1973) Arch. Biochem. Biophys. , vol.157 , pp. 580-587
    • Mo, Y.1    Harris, B.G.2    Gracy, R.W.3
  • 51
    • 0024959362 scopus 로고
    • An atypical hemebinding structure of cytochrome c1 of Euglena gracilis mitochondrial complex III
    • MUKAI, K., M. YOSHIDA, H. TOYOSAKI, Y. YAO, S. WAKABAYASHI, and H. MATSUBARA. 1989. An atypical hemebinding structure of cytochrome c1 of Euglena gracilis mitochondrial complex III. Eur. J. Biochem. 178:649-656.
    • (1989) Eur. J. Biochem. , vol.178 , pp. 649-656
    • Mukai, K.1    Yoshida, M.2    Toyosaki, H.3    Yao, Y.4    Wakabayashi, S.5    Matsubara, H.6
  • 52
    • 0000143331 scopus 로고    scopus 로고
    • Enzymes and compartmentation of core energy metabolism of anaerobic protists - A special case in eukaryotic evolution?
    • G. H. COOMBS, K. VICKERMAN, M. A. SLEIGH, and A. WARREN, eds. Kluwer, Dordrecht, the Netherlands
    • MÜLLER, M. 1998. Enzymes and compartmentation of core energy metabolism of anaerobic protists - a special case in eukaryotic evolution? Pp. 109-131 in G. H. COOMBS, K. VICKERMAN, M. A. SLEIGH, and A. WARREN, eds. Evolutionary relationships among protozoa. Kluwer, Dordrecht, the Netherlands.
    • (1998) Evolutionary Relationships among Protozoa , pp. 109-131
    • Müller, M.1
  • 54
    • 0032479390 scopus 로고    scopus 로고
    • Eubacterial origin of eukaryotic nuclear genes for chloroplast and cytosolic glucose-6-phosphate isomerase: Sampling eubacterial gene diversity in eukaryotic chromosomes through symbiosis
    • NOWITZKI, U., A. FLECHNER, J. KELLERMANN, M. HASEGAWA, C. SCHNARRENBERGER, and W. MARTIN. 1998. Eubacterial origin of eukaryotic nuclear genes for chloroplast and cytosolic glucose-6-phosphate isomerase: sampling eubacterial gene diversity in eukaryotic chromosomes through symbiosis. Gene 214:205-213.
    • (1998) Gene , vol.214 , pp. 205-213
    • Nowitzki, U.1    Flechner, A.2    Kellermann, J.3    Hasegawa, M.4    Schnarrenberger, C.5    Martin, W.6
  • 55
    • 0017366999 scopus 로고
    • Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: The glycosome
    • OPPERDOES, F. R., and P. BORST. 1977. Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: the glycosome. FEBS Lett. 80:360-364.
    • (1977) FEBS Lett. , vol.80 , pp. 360-364
    • Opperdoes, F.R.1    Borst, P.2
  • 56
    • 0031260066 scopus 로고    scopus 로고
    • Pyruvate kinase is present in Giardia intestinalis
    • PARK, J. H., P. J. SCHOFIELD, and M. R. EDWARDS. 1997. Pyruvate kinase is present in Giardia intestinalis. Exp. Parasitol. 87:153-156.
    • (1997) Exp. Parasitol. , vol.87 , pp. 153-156
    • Park, J.H.1    Schofield, P.J.2    Edwards, M.R.3
  • 57
    • 0027494836 scopus 로고
    • MUST, a computer package of management utilities for sequences and trees
    • PHILIPPE, H. 1993. MUST, a computer package of management utilities for sequences and trees. Nucleic Acids Res. 21: 5264-5272.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5264-5272
    • Philippe, H.1
  • 58
    • 0030956750 scopus 로고    scopus 로고
    • Cloning of fructose-1,6-bisphosphate aldolases from Euglena gracilis: Multiple recruitment of class I aldolase to chloroplasts and eubacterial origin of eukaryotic class II aldolase genes
    • PLAUMANN, M., B. PELZER-REITH, W. MARTIN, and C. SCHNARRENBERGER. 1997. Cloning of fructose-1,6-bisphosphate aldolases from Euglena gracilis: multiple recruitment of class I aldolase to chloroplasts and eubacterial origin of eukaryotic class II aldolase genes. Curr. Genet. 31:430-438.
    • (1997) Curr. Genet. , vol.31 , pp. 430-438
    • Plaumann, M.1    Pelzer-Reith, B.2    Martin, W.3    Schnarrenberger, C.4
  • 59
    • 0028280998 scopus 로고
    • Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage
    • READ, M., K. E. HICKS, P. F. SIMS, and J. E. HYDE. 1994. Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage. Eur. J. Biochem. 220:513-520.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 513-520
    • Read, M.1    Hicks, K.E.2    Sims, P.F.3    Hyde, J.E.4
  • 60
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • SAITOU, N., and M. NEI. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 62
    • 0039445025 scopus 로고    scopus 로고
    • Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia
    • SANCHEZ, L. B., H. G. MORRISON, M. L. SOGIN, and M. MÜLLER. 1999. Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia. Gene 233:225-231.
    • (1999) Gene , vol.233 , pp. 225-231
    • Sanchez, L.B.1    Morrison, H.G.2    Sogin, M.L.3    Müller, M.4
  • 64
    • 0028912631 scopus 로고
    • Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: Purification, characterization, and image processing
    • SCHURIG, H., K. RUTKAT, R. RACHEL, and R. JAENICKE. 1995. Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing. Protein Sci. 4:228-236.
    • (1995) Protein Sci. , vol.4 , pp. 228-236
    • Schurig, H.1    Rutkat, K.2    Rachel, R.3    Jaenicke, R.4
  • 66
    • 0031596609 scopus 로고    scopus 로고
    • i-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution
    • i-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution. J. Bacteriol. 180:2137-2143.
    • (1998) J. Bacteriol. , vol.180 , pp. 2137-2143
    • Siebers, B.1    Klenk, H.P.2    Hensel, R.3
  • 67
    • 0030046059 scopus 로고    scopus 로고
    • RNA: RNA interactions in the large subunit ribosomal RNA of Euglena gracilis
    • SMALLMAN, D. S., M. N. SCHNARE, and M. W. GRAY. 1996. RNA: RNA interactions in the large subunit ribosomal RNA of Euglena gracilis. Biochim. Biophys. Acta. 1305:1-6.
    • (1996) Biochim. Biophys. Acta. , vol.1305 , pp. 1-6
    • Smallman, D.S.1    Schnare, M.N.2    Gray, M.W.3
  • 68
    • 0003555695 scopus 로고
    • The origin of eukaryotes and evolution into major kingdoms
    • S. BENGSTON, ed. Columbia University Press, New York
    • SOGIN, M. 1994. The origin of eukaryotes and evolution into major kingdoms. Pp. 181-192 in S. BENGSTON, ed. Early life on earth. Columbia University Press, New York.
    • (1994) Early Life on Earth , pp. 181-192
    • Sogin, M.1
  • 69
    • 0032578482 scopus 로고    scopus 로고
    • Amitochondriate amoebae and the evolution of DNA-dependent RNA polymerase II
    • STILLER, J. W., E. C. DUFFIELD, and B. D. HALL. 1998. Amitochondriate amoebae and the evolution of DNA-dependent RNA polymerase II. Proc. Natl. Acad. Sci. USA 95:11769-11774.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11769-11774
    • Stiller, J.W.1    Duffield, E.C.2    Hall, B.D.3
  • 71
    • 0031004120 scopus 로고    scopus 로고
    • The coxl gene from Euglena gracilis: A protist mitochondrial gene without introns and genetic code modifications
    • TESSIER, L. H., H. VAN DER SPECK, J. M. GUALBERTO, and J. M. GRIENENBERGER. 1997. The coxl gene from Euglena gracilis: a protist mitochondrial gene without introns and genetic code modifications. Curr. Genet. 31:208-213.
    • (1997) Curr. Genet. , vol.31 , pp. 208-213
    • Tessier, L.H.1    Van Der Speck, H.2    Gualberto, J.M.3    Grienenberger, J.M.4
  • 72
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • THOMPSON, J. D., D. G. HIGGINS, and T. J. GIBSON. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 74
    • 0032834938 scopus 로고    scopus 로고
    • Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases
    • VORHOLT, J. A., L. CHISTOSERDOVA, S. M. STOLYAR, R. K. THAUER, and M. E. LIDSTROM. 1999. Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases. J. Bacteriol. 181:5750-5757.
    • (1999) J. Bacteriol. , vol.181 , pp. 5750-5757
    • Vorholt, J.A.1    Chistoserdova, L.2    Stolyar, S.M.3    Thauer, R.K.4    Lidstrom, M.E.5
  • 75
    • 0032414407 scopus 로고    scopus 로고
    • Towards a reconstruction of ancestral genomes by gene cluster alignment
    • WÄCHTERSHÄUSER, G. 1998. Towards a reconstruction of ancestral genomes by gene cluster alignment. Syst. Appl. Microbiol. 21:473-477.
    • (1998) Syst. Appl. Microbiol. , vol.21 , pp. 473-477
    • Wächtershäuser, G.1
  • 76
    • 0027964654 scopus 로고
    • 2+) complex of yeast enolase and the intermediate, phosphonoacetohydroxamate, at 2.1 Å resolution
    • 2+) complex of yeast enolase and the intermediate, phosphonoacetohydroxamate, at 2.1 Å resolution. Biochemistry 33:9333-9342.
    • (1994) Biochemistry , vol.33 , pp. 9333-9342
    • Wedekind, J.E.1    Reed, G.H.2    Rayment, I.3
  • 79
    • 0033161398 scopus 로고    scopus 로고
    • The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius
    • YANG, D., I. KUSSER, A. K. KOPKE, B. F. KOOP, and A. T. MATHESON. 1999. The structure and evolution of the ribosomal proteins encoded in the spc operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius. Mol. Phylogenet. Evol. 12:177-185.
    • (1999) Mol. Phylogenet. Evol. , vol.12 , pp. 177-185
    • Yang, D.1    Kusser, I.2    Kopke, A.K.3    Koop, B.F.4    Matheson, A.T.5
  • 80
    • 0031026931 scopus 로고    scopus 로고
    • Phylogenetic affinity of mitochondria of Euglena gracilis and kinetoplastids using cytochrome oxidase I and hsp60
    • YASUHIRA, S., and L. SIMPSON. 1997. Phylogenetic affinity of mitochondria of Euglena gracilis and kinetoplastids using cytochrome oxidase I and hsp60. J. Mol. Evol. 44:341-347.
    • (1997) J. Mol. Evol. , vol.44 , pp. 341-347
    • Yasuhira, S.1    Simpson, L.2
  • 81
    • 0030827288 scopus 로고    scopus 로고
    • Mechanism of enolase: The crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/ enolase-phosphoenolpyruv ate at 2.0 Å resolution
    • ZHANG, E., J. M. BREWER, W. MINOR, L. A. CARREIRA, and L. LEBIODA. 1997. Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/ enolase-phosphoenolpyruv ate at 2.0 Å resolution. Biochemistry 36:12526-12534.
    • (1997) Biochemistry , vol.36 , pp. 12526-12534
    • Zhang, E.1    Brewer, J.M.2    Minor, W.3    Carreira, L.A.4    Lebioda, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.